Faulhammer H G, Joshi R L
FEBS Lett. 1987 Jun 15;217(2):203-11. doi: 10.1016/0014-5793(87)80664-6.
In bacterial polypeptide synthesis aminoacyl-tRNA (aa-tRNA) bound to elongation factor Tu (EF-Tu) and GTP is part of a crucial intermediate ribonucleoprotein complex involved in the decoding of messenger RNA. The conformation and topology as well as the affinity of the macromolecules in this ternary aa-tRNA X EF-Tu X GTP complex are of fundamental importance for the nature of the interaction of the complex with the ribosome. The structural elements of aa-tRNA required for interaction with EF-Tu and GTP and the resulting functional implications are presented here.
在细菌多肽合成过程中，与延伸因子Tu（EF-Tu）和鸟苷三磷酸（GTP）结合的氨酰-tRNA（aa-tRNA）是参与信使核糖核酸解码的关键中间核糖核蛋白复合物的一部分。在这个三元aa-tRNA X EF-Tu X GTP复合物中，大分子的构象、拓扑结构以及亲和力对于该复合物与核糖体相互作用的性质至关重要。本文介绍了aa-tRNA与EF-Tu和GTP相互作用所需的结构元件以及由此产生的功能影响。
